4f6c
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Aureusimine biosynthetic cluster reductase domain== | |
| + | <StructureSection load='4f6c' size='340' side='right'caption='[[4f6c]], [[Resolution|resolution]] 2.81Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4f6c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_Mu50 Staphylococcus aureus subsp. aureus Mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F6C FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.812Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f6c OCA], [https://pdbe.org/4f6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f6c RCSB], [https://www.ebi.ac.uk/pdbsum/4f6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f6c ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0H3JX00_STAAM A0A0H3JX00_STAAM] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Through a number of strategies nonribosomal peptide assembly lines give rise to a metabolic diversity not possible by ribosomal synthesis. One distinction within nonribosomal assembly is that products are elaborated on an enzyme-tethered substrate, and their release is enzyme catalysed. Reductive release by NAD(P)H-dependent catalysts is one observed nonribosomal termination and release strategy. Here we probed the selectivity of a terminal reductase domain by using a full-length heterologously expressed nonribosomal peptide synthetase for the dipeptide aureusimine and were able to generate 17 new analogues. Further, we generated an X-ray structure of aureusimine terminal reductase to gain insight into the structural details associated with this enzymatic domain. | ||
| - | + | Heterologous expression and structural characterisation of a pyrazinone natural product assembly line.,Wyatt MA, Mok MC, Junop M, Magarvey NA Chembiochem. 2012 Nov 5;13(16):2408-15. doi: 10.1002/cbic.201200340. Epub 2012, Oct 15. PMID:23070851<ref>PMID:23070851</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4f6c" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Staphylococcus aureus subsp. aureus Mu50]] | ||
| + | [[Category: Junop M]] | ||
| + | [[Category: Mok M]] | ||
Current revision
Crystal structure of Aureusimine biosynthetic cluster reductase domain
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